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Allosteric disulphide bonds as reversible mechano-sensitive switches that control protein functions in the vasculature
Disulphide bonds are covalent linkages of two cysteine residues (R-S-S-R′) in proteins. Unlike peptide bonds, disulphide bonds are reversible in nature allowing cleaved bonds to reform. Disulphide bonds are important structural elements that stabilise protein conformation. They can be of catalytic f...
Guardat en:
| Publicat a: | Biophys Rev |
|---|---|
| Autors principals: | , |
| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
Springer Berlin Heidelberg
2019
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6557944/ https://ncbi.nlm.nih.gov/pubmed/31090016 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1007/s12551-019-00543-0 |
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